FMO DATABASE

FMODB ID: MN4QZ

Calculation Name: 1NG6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1NG6

Chain ID: A

ChEMBL ID:

UniProt ID: P54464

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1326985.617501
FMO2-HF: Nuclear repulsion	1267451.351413
FMO2-HF: Total energy	-59534.266088
FMO2-MP2: Total energy	-59705.266528

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:MET)

Summations of interaction energy for fragment #1(A:1:MET)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-10.951	-7.164	13.321	-4.616	-12.492	-0.046

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.067 / q_NPA : -0.028

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	LEU	0	0.093	0.039	2.801	-3.704	-1.335	0.377	-1.317	-1.429	-0.005
4	A	4	LEU	0	0.045	0.004	5.400	0.541	0.541	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.907	-0.940	2.268	-4.757	-3.422	6.004	-3.034	-4.306	-0.022
6	A	6	ARG	1	0.944	0.974	2.169	3.217	4.728	4.755	-2.366	-3.899	-0.003
7	A	7	LEU	0	0.044	0.022	2.812	3.519	0.716	0.110	3.227	-0.534	-0.001
8	A	8	ASN	0	0.018	0.009	6.352	0.148	0.148	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.015	-0.006	2.384	-4.629	-3.254	2.075	-1.126	-2.324	-0.015
10	A	10	ASP	-1	-0.767	-0.864	5.251	-1.451	-1.451	0.000	0.000	0.000	0.000
11	A	11	MET	0	-0.072	-0.029	6.792	0.028	0.028	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.972	0.976	8.788	-0.764	-0.764	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.003	0.018	7.741	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.044	0.003	9.531	0.021	0.021	0.000	0.000	0.000	0.000
15	A	15	MET	0	-0.051	-0.009	12.446	0.008	0.008	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.889	0.956	12.598	-0.167	-0.167	0.000	0.000	0.000	0.000
17	A	17	ASN	0	-0.044	-0.041	12.717	0.034	0.034	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.934	0.974	15.603	-0.057	-0.057	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.844	-0.901	14.259	-0.159	-0.159	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.961	0.959	15.783	0.066	0.066	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.877	-0.945	17.738	-0.161	-0.161	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.969	0.980	12.905	0.245	0.245	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.016	0.001	13.061	-0.040	-0.040	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.073	-0.040	14.238	0.001	0.001	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.046	0.032	14.055	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.034	0.024	9.382	-0.026	-0.026	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.937	0.953	12.020	0.087	0.087	0.000	0.000	0.000	0.000
28	A	28	MET	0	-0.065	-0.027	13.928	0.015	0.015	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.075	0.045	11.881	0.005	0.005	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.902	0.942	10.415	0.041	0.041	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.011	-0.007	12.252	0.007	0.007	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.041	-0.045	15.727	0.032	0.032	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.001	0.006	10.227	0.020	0.020	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.017	-0.018	12.995	0.045	0.045	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.004	-0.011	15.155	0.058	0.058	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.892	-0.940	17.024	-0.245	-0.245	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.035	0.015	15.640	0.024	0.024	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.003	0.000	17.776	0.044	0.044	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.888	0.946	20.411	0.216	0.216	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.046	-0.026	19.629	0.022	0.022	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.866	0.945	22.263	0.099	0.099	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.857	0.914	17.484	0.271	0.271	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.914	-0.955	14.708	-0.070	-0.070	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.051	-0.024	11.824	-0.044	-0.044	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.016	-0.010	12.961	0.067	0.067	0.000	0.000	0.000	0.000
46	A	46	THR	0	0.013	0.013	12.653	-0.059	-0.059	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.834	-0.943	7.802	-0.950	-0.950	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.820	-0.900	11.974	-0.521	-0.521	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.872	-0.921	15.337	-0.307	-0.307	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.911	-0.963	9.714	-1.427	-1.427	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.005	0.002	12.833	0.016	0.016	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.057	-0.021	15.076	0.065	0.065	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.026	-0.009	15.167	0.047	0.047	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.023	0.009	10.963	0.049	0.049	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.029	0.008	15.433	0.056	0.056	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.894	0.964	18.632	0.355	0.355	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.854	-0.908	16.217	-0.315	-0.315	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.040	0.019	17.682	0.039	0.039	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.828	0.897	19.536	0.253	0.253	0.000	0.000	0.000	0.000
60	A	60	GLN	0	-0.020	-0.001	21.650	0.034	0.034	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.848	0.917	18.288	0.345	0.345	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.964	0.994	22.560	0.330	0.330	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.858	-0.926	25.113	-0.189	-0.189	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.001	-0.003	25.951	0.016	0.016	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.017	0.008	25.499	0.014	0.014	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.003	-0.001	28.141	0.007	0.007	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.948	-0.977	30.942	-0.132	-0.132	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.010	-0.026	27.703	0.011	0.011	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.016	-0.005	32.304	0.011	0.011	0.000	0.000	0.000	0.000
70	A	70	ASN	0	0.000	0.004	33.893	0.007	0.007	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.058	-0.027	35.427	0.007	0.007	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.034	-0.009	36.622	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.805	0.896	33.161	0.097	0.097	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.097	0.016	32.553	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.750	-0.844	30.858	-0.105	-0.105	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.080	-0.042	28.763	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.005	0.017	27.681	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.874	-0.942	27.001	-0.150	-0.150	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.836	0.923	23.725	0.142	0.142	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.006	-0.010	22.932	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	81	GLN	0	0.006	0.003	22.332	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.949	0.975	20.631	0.142	0.142	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.908	-0.963	18.393	-0.264	-0.264	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.035	-0.012	17.476	-0.052	-0.052	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.805	-0.895	17.658	-0.326	-0.326	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.114	-0.049	13.212	-0.044	-0.044	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.036	-0.030	13.153	-0.090	-0.090	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.902	-0.959	13.282	-0.511	-0.511	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.028	0.012	9.642	-0.066	-0.066	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.193	-0.146	6.371	-0.131	-0.131	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.043	-0.014	10.151	-0.140	-0.140	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.056	-0.006	13.087	0.001	0.001	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.884	-0.949	15.033	-0.344	-0.344	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.098	-0.068	17.500	0.055	0.055	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.003	0.005	20.512	0.022	0.022	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.009	0.005	24.004	0.012	0.012	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.837	-0.933	27.061	-0.167	-0.167	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.924	-0.963	29.656	-0.146	-0.146	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.823	-0.907	25.992	-0.251	-0.251	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.010	-0.006	25.886	0.002	0.002	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.841	0.896	28.266	0.159	0.159	0.000	0.000	0.000	0.000
102	A	102	THR	0	-0.002	0.015	30.551	0.013	0.013	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.027	0.012	24.911	0.009	0.009	0.000	0.000	0.000	0.000
104	A	104	VAL	0	-0.025	-0.005	29.113	0.006	0.006	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.016	-0.004	30.941	0.009	0.009	0.000	0.000	0.000	0.000
106	A	106	GLH	0	-0.049	-0.050	29.245	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.004	-0.018	28.593	0.003	0.003	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.016	-0.008	31.018	0.007	0.007	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.021	-0.013	34.240	0.008	0.008	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.797	-0.834	29.351	-0.146	-0.146	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.045	-0.016	31.149	0.006	0.006	0.000	0.000	0.000	0.000
112	A	112	GLY	0	-0.013	-0.011	34.257	0.006	0.006	0.000	0.000	0.000	0.000
113	A	113	ALA	0	-0.076	-0.019	35.688	0.004	0.004	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.004	0.002	37.636	0.002	0.002	0.000	0.000	0.000	0.000
115	A	115	SER	0	0.026	0.027	40.387	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.933	0.950	37.960	0.100	0.100	0.000	0.000	0.000	0.000
117	A	117	ALA	0	-0.017	0.011	37.675	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.828	-0.925	36.445	-0.091	-0.091	0.000	0.000	0.000	0.000
119	A	119	MET	0	0.010	-0.008	32.409	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	120	GLY	0	-0.015	-0.001	31.410	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.945	0.976	30.256	0.089	0.089	0.000	0.000	0.000	0.000
122	A	122	VAL	0	0.009	0.008	30.281	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	123	MET	0	0.000	-0.013	26.679	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.004	0.005	25.881	-0.018	-0.018	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.009	0.005	25.084	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	126	ILE	0	-0.003	0.004	25.502	-0.011	-0.011	0.000	0.000	0.000	0.000
127	A	127	MET	0	0.008	0.007	21.203	-0.020	-0.020	0.000	0.000	0.000	0.000
128	A	128	PRO	0	-0.046	-0.022	19.616	-0.043	-0.043	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.791	0.874	19.473	0.157	0.157	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.009	-0.004	21.404	-0.016	-0.016	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.867	0.940	15.305	0.443	0.443	0.000	0.000	0.000	0.000
132	A	132	GLY	0	0.006	-0.003	16.530	-0.045	-0.045	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.955	0.991	17.570	0.407	0.407	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.059	0.035	19.963	0.036	0.036	0.000	0.000	0.000	0.000
135	A	135	ASP	-1	-0.856	-0.942	22.135	-0.297	-0.297	0.000	0.000	0.000	0.000
136	A	136	GLY	0	0.049	0.017	23.221	0.021	0.021	0.000	0.000	0.000	0.000
137	A	137	SER	0	-0.009	-0.004	24.797	0.026	0.026	0.000	0.000	0.000	0.000
138	A	138	LEU	0	0.003	0.002	27.339	0.019	0.019	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.049	0.030	23.462	0.018	0.018	0.000	0.000	0.000	0.000
140	A	140	ASN	0	-0.006	-0.015	27.353	0.026	0.026	0.000	0.000	0.000	0.000
141	A	141	LYS	1	0.946	0.985	30.101	0.164	0.164	0.000	0.000	0.000	0.000
142	A	142	LEU	0	-0.041	-0.037	30.245	0.014	0.014	0.000	0.000	0.000	0.000
143	A	143	VAL	0	0.047	0.027	29.877	0.010	0.010	0.000	0.000	0.000	0.000
144	A	144	SER	0	0.000	-0.015	32.944	0.013	0.013	0.000	0.000	0.000	0.000
145	A	145	SER	0	-0.091	-0.055	35.613	0.010	0.010	0.000	0.000	0.000	0.000
146	A	146	GLN	0	-0.047	0.001	35.932	0.012	0.012	0.000	0.000	0.000	0.000
147	A	147	LEU	0	-0.023	0.017	34.944	0.005	0.005	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.006	-0.021	38.822	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:MET)